Erratum to: JMJD2A-dependent silencing of Sp1 in advanced breast cancer promotes metastasis by downregulation of DIRAS3 (Breast Cancer Research and Treatment, (2014), 147, (487-500), DOI:10.1007/s10549-014-3083-7);JMJD2A-dependent silencing of Sp1 in advanced breast cancer promotes metastasis by downregulation of DIRAS3

Breast Cancer Research and Treatment

Volumn 147, Issue 3, 2014, Pages 487-500

  Li, Liliang ^a,b   Gao, Pan ^a   Li, Yuhua ^a   Shen, Yiwen ^a   Xie, Jianhui ^a   Sun, Daming ^c   Xue, Aimin ^a   Zhao, Ziqin ^a   Xu, Zude ^a   Zhang, Mingchang ^a   Li, Beixu ^a   Jiang, Jieqing ^a  

^a FUDAN UNIVERSITY   (China)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^c EAST CHINA UNIVERSITY OF POLITICAL SCIENCE AND LAW   (China)

Author keywords

Breast cancer; DIRAS3; Invasion; JMJD2A; Migration; Sp1

Indexed keywords

GTP BINDING RAS LIKE 3; HISTONE DEMETHYLASE; JUMONJI DOMAIN CONTAINING 2A; TRANSCRIPTION FACTOR SP1; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; DIRAS3 PROTEIN, HUMAN; KDM4A PROTEIN, HUMAN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

AGE; ARTICLE; AUTOREGULATION; BREAST CANCER; BREAST CANCER CELL LINE; BREAST METASTASIS; CANCER STAGING; CANCER TISSUE; CELL INVASION; CELL MIGRATION; CHROMATIN IMMUNOPRECIPITATION; CO-IMMUNOPRECIPITATION; CONTROLLED STUDY; CORRELATION ANALYSIS; DOWN REGULATION; FEMALE; GENE DELETION; GENE EXPRESSION; GENE OVEREXPRESSION; GENE REGULATORY NETWORK; GENE SILENCING; GENE TARGETING; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; IMMUNOPRECIPITATION; LUCIFERASE ASSAY; LYMPH NODE METASTASIS; MAJOR CLINICAL STUDY; MUTAGENESIS; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; QUANTITATIVE ANALYSIS; REPORTER GENE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; TRANSCRIPTION INITIATION; TUMOR VOLUME; UPREGULATION; WESTERN BLOTTING; WOUND HEALING; BREAST TUMOR; CELL MOTION; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MIDDLE AGED; PATHOLOGY; PROMOTER REGION; TUMOR CELL LINE;

BREAST NEOPLASMS; CELL LINE, TUMOR; CELL MOVEMENT; DOWN-REGULATION; FEMALE; GENE EXPRESSION REGULATION, NEOPLASTIC; GENE KNOCKDOWN TECHNIQUES; GENE SILENCING; HUMANS; JUMONJI DOMAIN-CONTAINING HISTONE DEMETHYLASES; MIDDLE AGED; PROMOTER REGIONS, GENETIC; RHO GTP-BINDING PROTEINS; SP1 TRANSCRIPTION FACTOR;

EID: 84918517080     PISSN: 01676806     EISSN: 15737217     Source Type: Journal    
DOI: 10.1007/s10549-016-3714-2     Document Type: Erratum

References (39)

1. Abuidris DO, Elsheikh A, Ali M, Musa H, Elgaili E, Ahmed AO, Sulieman I, Mohammed SI (2013) Breast-cancer screening with trained volunteers in a rural area of Sudan: a pilot study. Lancet Oncol 14(4):363–370
2. Lee EY, Muller WJ (2010) Oncogenes and tumor suppressor genes. Cold Spring Harb Perspect Biol 2(10):a3236
3. Li L, Davie JR (2010) The role of Sp1 and Sp3 in normal and cancer cell biology. Ann Anat 192(5):275–283
4. Kadonaga JT, Carner KR, Masiarz FR, Tjian R (1987) Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell 51(6):1079–1090
5. Guo D, Wu B, Yan J, Li X, Sun H, Zhou D (2012) A possible gene silencing mechanism: hypermethylation of the Keap1 promoter abrogates binding of the transcription factor Sp1 in lung cancer cells. Biochem Biophys Res Commun 428(1):80–85
6. Hsu TI, Wang MC, Chen SY, Yeh YM, Su WC, Chang WC, Hung JJ (2012) Sp1 expression regulates lung tumor progression. Oncogene 31(35):3973–3988
7. Yue L, Li L, Liu F, Hu N, Zhang W, Bai X et al (2013) The oncoprotein HBXIP activates transcriptional coregulatory protein LMO4 via Sp1 to promote proliferation of breast cancer cells. Carcinogenesis 34(4):927–935
8. Banerjee S, Sangwan V, McGinn O, Chugh R, Dudeja V, Vickers SM, Saluja AK (2013) Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1. J Biol Chem 288(47):33927–33938
9. Black AR, Black JD, Azizkhan-Clifford J (2001) Sp1 and kruppel-like factor family of transcription factors in cell growth regulation and cancer. J Cell Physiol 188(2):143–160
10. Zheng Y, Ritzenthaler JD, Sun X, Roman J, Han S (2009) Prostaglandin E2 stimulates human lung carcinoma cell growth through induction of integrin-linked kinase: the involvement of EP4 and Sp1. Cancer Res 69(3):896–904
11. Jiang Y, Wang L, Gong W, Wei D, Le X, Yao J et al (2004) A high expression level of insulin-like growth factor I receptor is associated with increased expression of transcription factor Sp1 and regional lymph node metastasis of human gastric cancer. Clin Exp Metastasis 21(8):755–764
12. Mitchell DC, Stafford LJ, Li D, Bar-Eli M, Liu M (2007) Transcriptional regulation of KiSS-1 gene expression in metastatic melanoma by specificity protein-1 and its coactivator DRIP-130. Oncogene 26(12):1739–1747
13. DeFino MC, Wacker JL, Lyssand JS, Wang EH, Hague C (2010) Differential regulation of GPR54 transcription by specificity protein-1 and partial estrogen response element in mouse pituitary cells. Biochem Biophys Res Commun 393(4):603–608
14. Bu Y, Gao L, Gelman IH (2011) Role for transcription factor TFII-I in the suppression of SSeCKS/Gravin/Akap12 transcription by Src. Int J Cancer 128(8):1836–1842
15. Covington KR, Brusco L, Barone I, Tsimelzon A, Selever J, Corona-Rodriguez A, Brown P, Kumar R, Hilsenbeck SG, Fuqua SA (2013) Metastasis tumor-associated protein 2 enhances metastatic behavior and is associated with poor outcomes in estrogen receptor-negative breast cancer. Breast Cancer Res Treat 141:375–384
16. Perera RM, Bardeesy N (2012) On oncogenes and tumor suppressor genes in the mammary gland. Cold Spring Harb Perspect Biol 4:a013466. doi:10.1101/cshperspect.a013466
17. Yu Y, Xu F, Peng H, Fang X, Zhao S, Li Y et al (1999) NOEY2 (DIRAS3), an imprinted putative tumor suppressor gene in ovarian and breast carcinomas. Proc Natl Acad Sci USA 96(1):214–219
18. Wang L, Hoque A, Luo RZ, Yuan J, Lu Z, Nishimoto A et al (2003) Loss of the expression of the tumor suppressor gene DIRAS3 is associated with progression of breast cancer. Clin Cancer Res 9(10 Pt 1):3660–3666
19. Janssen EA, Ovestad IT, Skaland I, Soiland H, Gudlaugsson E, Kjellevold KH et al (2009) LOH at 1p31 (DIRAS3) and proliferation in lymph node-negative breast cancer. Cell Oncol 31(5):335–343
20. Li Y, Liu M, Zhang Y, Han C, You J, Yang J et al (2013) Effects of DIRAS3 on breast cancer cell biological behavior regulated by microRNA-221. Tumour Biol 34(6):3545–3554
21. Yu Y, Luo R, Lu Z, Wei FW, Badgwell D, Issa JP et al (2006) Biochemistry and biology of DIRAS3 (DIRAS3), an imprinted tumor suppressor gene whose expression is lost in ovarian and breast cancers. Methods Enzymol 407:455–468
22. Klingauf M, Beck M, Berge U, Turgay Y, Heinzer S, Horvath P, Kroschewski R (2013) The tumour suppressor DiRas3 interacts with C-RAF and downregulates MEK activity to restrict cell migration. Biol Cell 105(2):91–107
23. Lu Z, Luo RZ, Peng H, Huang M, Nishmoto A, Hunt KK et al (2006) E2F-HDAC complexes negatively regulate the tumor suppressor gene DIRAS3 in breast cancer. Oncogene 25(2):230–239
24. Feng W, Lu Z, Luo RZ, Zhang X, Seto E, Liao WS, Yu Y (2007) Multiple histone deacetylases repress tumor suppressor gene DIRAS3 in breast cancer. Int J Cancer 120(8):1664–1668
25. Luo RZ, Peng H, Xu F, Bao J, Pang Y, Pershad R et al (2001) Genomic structure and promoter characterization of an imprinted tumor suppressor gene DIRAS3. Biochim Biophys Acta 1519(3):216–222
26. Safe S, Abdelrahim M (2005) Sp transcription factor family and its role in cancer. Eur J Cancer 41(16):2438–2448
27. Yang X, Wang J, Liu S, Yan Q (2014) HSF1 and Sp1 regulate FUT4 gene expression and cell proliferation in breast cancer cells. J Cell Biochem 115(1):168–178
28. Badgwell DB, Lu Z, Le K, Gao F, Yang M, Suh GK et al (2012) The tumor-suppressor gene DIRAS3 (DIRAS3) suppresses ovarian cancer cell migration through inhibition of the Stat3 and FAK/Rho signaling pathways. Oncogene 31(1):68–79
29. Li LL, Xue AM, Li BX, Shen YW, Li YH, Luo CL et al (2014) JMJD2A contributes to breast cancer progression through transcriptional repression of the tumor suppressor DIRAS3. Breast Cancer Res 16(3):R56. doi:10.1186/bcr3667
30. Nicolas M, Noe V, Jensen KB, Ciudad CJ (2001) Cloning and characterization of the 5′-flanking region of the human transcription factor Sp1 gene. J Biol Chem 276(25):22126–22132
31. Gray SG, Iglesias AH, Lizcano F, Villanueva R, Camelo S, Jingu H et al (2005) Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem 280(31):28507–28518
32. Whetstine JR, Nottke A, Lan F, Huarte M, Smolikov S, Chen Z et al (2006) Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell 125(3):467–481
33. Kwak HJ, Park MJ, Cho H, Park CM, Moon SI, Lee HC et al (2006) Transforming growth factor-beta1 induces tissue inhibitor of metalloproteinase-1 expression via activation of extracellular signal-regulated kinase and Sp1 in human fibrosarcoma cells. Mol Cancer Res 4(3):209–220
34. Klose RJ, Yamane K, Bae Y, Zhang D, Erdjument-Bromage H, Tempst P, Wong J, Zhang Y (2006) The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 442(7100):312–316
35. Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM (2006) Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312(5774):748–751
36. Lee J, Thompson JR, Botuyan MV, Mer G (2008) Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat Struct Mol Biol 15(1):109–111
37. Mallette FA, Richard S (2012) JMJD2A promotes cellular transformation by blocking cellular senescence through transcriptional repression of the tumor suppressor CHD5. Cell Rep 2(5):1233–1243
38. Zhang D, Yoon HG, Wong J (2005) JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2). Mol Cell Biol 25(15):6404–6414
39. Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (1998) The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 95(2):279–289